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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities

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Author(s):
Amadeu Megale, Angela Alice [1] ; Magnoli, Fabio Carlos [1] ; Kuniyoshi, Alexandre Kazuo [1] ; Iwai, Leo Kei [2] ; Tambourgi, Denise V. [1] ; Portaro, Fernanda C. V. [1] ; da Silva, Wilmar Dias [1]
Total Authors: 7
Affiliation:
[1] Butantan Inst, Immunochem Lab, BR-05503900 Sao Paulo - Brazil
[2] Butantan Inst, Special Lab Appl Toxinol, Ctr Toxins Immune Response & Cell Signaling CeTIC, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 2
Document type: Journal article
Source: Journal of Venomous Animals and Toxins including Tropical Diseases; v. 24, DEC 13 2018.
Web of Science Citations: 1
Abstract

BackgroundBitis arietans is a venomous snake found in sub-Saharan Africa and in parts of Morocco and Saudi Arabia. The envenomation is characterized by local and systemic reactions including pain, blistering, edema and tissue damage, besides hemostatic and cardiovascular disturbances, which can cause death or permanent disabilities in its victims. However, the action mechanisms that provoke these effects remain poorly understood, especially the activities of purified venom components. Therefore, in order to elucidate the molecular mechanisms that make the Bitis arietans venom so potent and harmful to human beings, this study reports the isolation and biochemical characterization of a snake venom serine protease (SVSP).MethodsSolubilized venom was fractionated by molecular exclusion chromatography and the proteolytic activity was determined using fluorescent substrates. The peaks that showed serine protease activity were determined by blocking the proteolytic activity with site-directed inhibitors. In sequence, the fraction of interest was submitted to another cycle of molecular exclusion chromatography. The purified serine protease was identified by mass spectrometry and characterized biochemically and immunochemically.ResultsA serine protease of 33kDa with fibrinogen-degrading and kinin-releasing activities was isolated, described, and designated herein as Kn-Ba. The experimental Butantan Institute antivenom produced against Bitis arietans venom inhibited the Kn-Ba activity.ConclusionsThe in vitro activities of Kn-Ba can be correlated with the capacity of the venom to provoke bleeding and clotting disorders as well as hypotension, which are common symptoms presented by envenomed victims. Obtaining satisfactory Kn-Ba inhibition through the experimental antivenom is important, given the WHO's recommendation of immunotherapy in cases of human accidents with venomous snakes. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 13/15344-7 - Efficacy of the bothropic antivenom from Butantan Institute: obtention, characterization and neutralization of serinepeptidases from the venom of Bothrops jararaca
Grantee:Alexandre Kazuo Kuniyoshi
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 15/15364-3 - Toxic potential analysis of proteases and peptides present in scorpion Tityus serrulatus venom and the blockage capacity of commercial antivenoms: enhancing the knowledge of venom and its mechanism of action
Grantee:Fernanda Calheta Vieira Portaro
Support type: Regular Research Grants